Faculty Opinions recommendation of A polyketide synthase in glycopeptide biosynthesis: the biosynthesis of the non-proteinogenic amino acid (S)-3,5-dihydroxyphenylglycine.

The legume Oxytropis sericea hosts a fungal endophyte, Alternaria oxytropis, which produces secondary metabolites (SM), including the toxin swainsonine. Polyketide synthase (PKS) and non-ribosomal peptide synthase (NRPS) enzymes are associated with biosynthesis of fungal SM. To better understand the origins of the SM, an unannotated genome of A. oxytropis was assessed for protein sequences similar to known PKS and NRPS enzymes of fungi. Contigs exhibiting identity with known genes were analyzed at nucleotide and protein levels using available databases. Software were used to identify PKS and NRPS domains and predict identity and function. Confirmation of sequence for selected gene sequences was accomplished using PCR. Thirteen PKS, 5 NRPS, and 4 PKS-NRPS hybrids were identified and characterized with functions including swainsonine and melanin biosynthesis. Phylogenetic relationships among closest amino acid matches with Alternaria spp. were identified for seven highly conserved PKS and NRPS, including melanin synthesis. Three PKS and NRPS were most closely related to other fungi within the Pleosporaceae family, while five PKS and PKS-NRPS were closely related to fungi in the Pleosporales order. However, seven PKS and PKS-NRPS showed no identity with fungi in the Pleosporales or the class Dothideomycetes, suggesting a different evolutionary origin for those genes.

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Synthesis and anti-phlogistic potency of some new non-proteinogenic amino acid conjugates of ?Diclofenac?

Amino Acids ◽

10.1007/bf01388181 ◽

1999 ◽

Vol 16 (3-4) ◽

pp. 425-440 ◽

Cited By ~ 7

Author(s):

M. H. Abo-Ghalia ◽

A. M. Shalaby ◽

W. I. El-Eraqi ◽

H. M. Awad

Keyword(s):

Amino Acid ◽

Amino Acid Conjugates ◽

Proteinogenic Amino Acid

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Analysis of Proteinogenic Amino Acid and Starch Labeling by 2D NMR

Plant Metabolic Flux Analysis - Methods in Molecular Biology ◽

10.1007/978-1-62703-688-7_6 ◽

2013 ◽

pp. 87-105 ◽

Cited By ~ 2

Author(s):

Quyen Truong ◽

Jacqueline V. Shanks

Keyword(s):

Amino Acid ◽

2D Nmr ◽

Proteinogenic Amino Acid

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Deciphering Biosynthetic Enzymes Leading to 4-Chloro-6-Methyl-5,7-Dihydroxyphenylglycine, a Non-Proteinogenic Amino Acid in Totopotensamides

ACS Chemical Biology ◽

10.1021/acschembio.9b00997 ◽

2020 ◽

Vol 15 (3) ◽

pp. 766-773 ◽

Cited By ~ 1

Author(s):

Bin Tan ◽

Qingbo Zhang ◽

Yiguang Zhu ◽

Hongbo Jin ◽

Liping Zhang ◽

...

Keyword(s):

Amino Acid ◽

Biosynthetic Enzymes ◽

Proteinogenic Amino Acid

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A concise preparation of the non-proteinogenic amino acid l-kynurenine

Tetrahedron Letters ◽

10.1016/j.tetlet.2012.09.055 ◽

2012 ◽

Vol 53 (47) ◽

pp. 6430-6432 ◽

Cited By ~ 13

Author(s):

Laurens H.J. Kleijn ◽

Frederike M. Müskens ◽

Sabine F. Oppedijk ◽

Gerjan de Bruin ◽

Nathaniel I. Martin

Keyword(s):

Amino Acid ◽

Proteinogenic Amino Acid

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Structural and evolutionary relationships of “AT-less” type I polyketide synthase ketosynthases

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1515460112 ◽

2015 ◽

Vol 112 (41) ◽

pp. 12693-12698 ◽

Cited By ~ 37

Author(s):

Jeremy R. Lohman ◽

Ming Ma ◽

Jerzy Osipiuk ◽

Boguslaw Nocek ◽

Youngchang Kim ◽

...

Keyword(s):

Amino Acid ◽

Substrate Specificity ◽

Polyketide Synthase ◽

Acyl Carrier Protein ◽

Structural Diversity ◽

Type I ◽

Substrate Specificities ◽

In Trans ◽

Canonical Type ◽

Insight Into

Acyltransferase (AT)-less type I polyketide synthases (PKSs) break the type I PKS paradigm. They lack the integrated AT domains within their modules and instead use a discrete AT that acts in trans, whereas a type I PKS module minimally contains AT, acyl carrier protein (ACP), and ketosynthase (KS) domains. Structures of canonical type I PKS KS-AT didomains reveal structured linkers that connect the two domains. AT-less type I PKS KSs have remnants of these linkers, which have been hypothesized to be AT docking domains. Natural products produced by AT-less type I PKSs are very complex because of an increased representation of unique modifying domains. AT-less type I PKS KSs possess substrate specificity and fall into phylogenetic clades that correlate with their substrates, whereas canonical type I PKS KSs are monophyletic. We have solved crystal structures of seven AT-less type I PKS KS domains that represent various sequence clusters, revealing insight into the large structural and subtle amino acid residue differences that lead to unique active site topologies and substrate specificities. One set of structures represents a larger group of KS domains from both canonical and AT-less type I PKSs that accept amino acid-containing substrates. One structure has a partial AT-domain, revealing the structural consequences of a type I PKS KS evolving into an AT-less type I PKS KS. These structures highlight the structural diversity within the AT-less type I PKS KS family, and most important, provide a unique opportunity to study the molecular evolution of substrate specificity within the type I PKSs.

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The first supramolecular peptidic hydrogelator containing taurine

Chemical Communications ◽

10.1039/c3cc48832b ◽

2014 ◽

Vol 50 (21) ◽

pp. 2772-2774 ◽

Cited By ~ 26

Author(s):

Yi Kuang ◽

Yuan Gao ◽

Junfeng Shi ◽

Jie Li ◽

Bing Xu

Keyword(s):

Amino Acid ◽

Rich Phase ◽

Proteinogenic Amino Acid ◽

A Cell ◽

Phase Behaviors ◽

Dipeptide Derivative

The conjugation of taurine, a non-proteinogenic amino acid, with a dipeptide derivative affords a cell compatible, small molecular hydrogelator that self-assembles in water to exhibit rich phase behaviors.

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The Molecular Mass and Isoelectric Point of Plant Proteomes

10.21203/rs.2.10723/v1 ◽

2019 ◽

Author(s):

Tapan Kumar Kumar Mohanta ◽

Abdulatif Khan ◽

Abeer Hashem ◽

Elsayed Fathi Abd_Allah ◽

Ahmed Al-Harrasi

Keyword(s):

Amino Acids ◽

Molecular Weight ◽

Amino Acid ◽

Molecular Mass ◽

Plant Species ◽

Isoelectric Point ◽

Polyketide Synthase ◽

Type I ◽

Plant Proteins ◽

Higher Plant

Abstract Background Cell contain diverse array of proteins with different molecular weight and isoelectric point (pI). The molecular weight and pI of protein play important role in determining the molecular biochemical function. Therefore, it was important to understand the detail regarding the molecular weight and pI of the plant proteins. Results A proteome-wide analysis of plant proteomes from 145 species revealed a pI range of 1.99 (epsin) to 13.96 (hypothetical protein). The spectrum of molecular mass of the plant proteins varied from 0.54 to 2236.8 kDa. A putative Type-I polyketide synthase (22244 amino acids) in Volvox carteri was found to be the largest protein in the plant kingdom. However, Type-I polyketide synthase was not found in higher plant species. Titin (806.46 kDa) and misin/midasin (730.02 kDa) were the largest proteins identified in higher plant species. The pI and molecular weight of the plant proteins showed a trimodal distribution. An acidic pI (56.44% of proteins) was found to be predominant over a basic pI (43.34% of proteins) and the abundance of acidic pI proteins was higher in unicellular algae species relative to multicellular higher plants. In contrast, the seaweed, Porphyra umbilicalis, possesses a higher proportion of basic pI proteins (70.09%). Plant proteomes were also found to contain selenocysteine (Sec), amino acid that was found only in lower eukaryotic aquatic plant lineage. Amino acid composition analysis showed Leu was high and Trp was low abundant amino acids in the plant proteome. Additionally, the plant proteomes also possess ambiguous amino acids Xaa (unknown), Asx (asparagine or aspartic acid), Glx (glutamine or glutamic acid), and Xle (leucine or isoleucine) as well. Conclusion The diverse molecular weight and isoelectric point range of plant proteome will be helpful to understand their biochemical and functional aspects. The presence of selenocysteine proteins in lower eukaryotic organism is of interest and their expression in higher plant system can help us to understand their functional role.

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Unique features of the ketosynthase domain in a nonribosomal peptide synthetase–polyketide synthase hybrid enzyme, tenuazonic acid synthetase 1

Journal of Biological Chemistry ◽

10.1074/jbc.ra120.013105 ◽

2020 ◽

Vol 295 (33) ◽

pp. 11602-11612 ◽

Cited By ~ 1

Author(s):

Choong-Soo Yun ◽

Kazuki Nishimoto ◽

Takayuki Motoyama ◽

Takeshi Shimizu ◽

Tomoya Hino ◽

...

Keyword(s):

Amino Acid ◽

Polyketide Synthase ◽

Binding Pocket ◽

Single Amino Acid ◽

Tenuazonic Acid ◽

Nonribosomal Peptide ◽

Hybrid Enzyme ◽

Peptide Synthetases ◽

Multienzyme Complexes ◽

Ketosynthase Domain

Many microbial secondary metabolites are produced by multienzyme complexes comprising nonribosomal peptide synthetases (NRPSs) and polyketide synthases (PKSs). The ketosynthase (KS) domains of polyketide synthase normally catalyze the decarboxylative Claisen condensation of acyl and malonyl blocks to extend the polyketide chain. However, the terminal KS domain in tenuazonic acid synthetase 1 (TAS1) from the fungus Pyricularia oryzae conducts substrate cyclization. Here, we report on the unique features of the KS domain in TAS1. We observed that this domain is monomeric, not dimeric as is typical for KSs. Analysis of a 1.68-Å resolution crystal structure suggests that the substrate cyclization is triggered via proton abstraction from the active methylene moiety in the substrate by a catalytic His-322 residue. Additionally, we show that TAS1 KS promiscuously accepts aminoacyl substrates and that this promiscuity can be increased by a single amino acid substitution in the substrate-binding pocket of the enzyme. These findings provide insight into a KS domain that accepts the amino acid–containing substrate in an NRPS–PKS hybrid enzyme and provide hints to the substrate cyclization mechanism performed by the KS domain in the biosynthesis of the mycotoxin tenuazonic acid.

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